Homework Answers
Michaelis menton equation is first used to draw the correct plot
between Vo and [S]. Then, to know the reason of given plot being
wrong.![in Michaelis - Menten equation is given by - rate : Vo Vmax [f1 - km test and we get the following plat : • At low [s ] react](http://img.homeworklib.com/questions/966219b0-d9d2-11eb-a6ac-a5c232229480.png?x-oss-process=image/resize,w_560)
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need help with this problem, please!
CHEM2201: Introduction to Biochemical Principles Problem Set 5 1....
(I need help with part C, Drawing the expected Michaelis-Menten plot; Do NOT draw the Lineweaver-Burk...
(I need help with part C, Drawing the expected Michaelis-Menten plot; Do NOT draw the Lineweaver-Burk plot. thanks!) 1. Michaelis-Menten kinetics- use the M-M equation to answer the following: a. An enzyme (5 µM) has a Vmax of 450 mM/min. What is kcat? b. When the substrate concentration is 50 mM, the initial velocity (V0) was measured to be 375 mM/min. Under the conditions described above, calculate the KM. c. Draw the expected Michaelis-Menten plot (label your axes and include...
To determine the kinetic characteristics of an enzyme you used 1 nmol/L of enzyme in a...
To determine the kinetic characteristics of an enzyme you used 1 nmol/L of enzyme in a series of assays where you measured the rate of reactions as you varied the concentration of substrate in each assay (Table A). Estimate from a Michaelis-Menten plot approximate values for Vmax, KM, Kcat, and the specificity constant for this enzyme and substrate. (The only information that is given is this paragraph and the table below). Table 1: [S] (μM) v (μmol/L/min) 0 0 5...
3. Why is an allosteric enzyme more sensitive to substrate concentration around Km values than a...
3. Why is an allosteric enzyme more sensitive to substrate concentration around Km values than a Michaelis-Menten enzyme with the same Vmax? 4. Explain how pH and temperature influence enzyme activity. ( A Lineweaver-Burk (double reciprocal) plot was used to compare the effects of three different reversible inhibitors (A, B and C) on an enzyme. The plot of 1/V vs 1/[S] for the enzyme with no inhibitor is shown in a solid black line. The plot of 1/V vs 1/[S]...
Please show work and answer. my professor gave this hint to us to solve the problem....
Please show work and answer.
my professor gave this hint to us to solve the problem.
He also said that I could find the relationship between S and
Km and substitute that into the Michaelis-Menten equation.
6. The Km of RBC GLUT1 for glucose is 18 mg/dL while the Km for liver GLUT2 is 360 mg/dL. At a blood glucose concentration of 60 mg/dL, GLUT1 and GLUT2 are working at what percentage of their Vmax? A. GLUT1 at 75% Vmax...
That's all the information. Something like this. Something like this. I don't know why you need...
That's all the information. Something like this.
Something like this. I don't know why you need more
information.
Its already plotted the (Enzyme) if i cant be answered
close the question, so I may repost it again. Just asked the
professor so i don't know.
6. The Michaelis-Menten curve for enzyme X is shown below for substrate A. Indicate where on the plot you would determine Keat, Kn and kca/Km. 500 1500 2000 1000 substrate A, UM We were unable...
i need help with all question 5 please! thank you Question 5: Use the data below...
i need help with all question 5 please! thank you
Question 5: Use the data below to construct a Michaelis-Menton curve of velocity vs. [S]. This is quite easy to do in Excel. Vo (UM/s) a) Estimate Vmax from your curve. b) Describe any difficulty you have in completing part (a). Is the enzyme saturated at the highest [S]? c) Using your Vmax estimate, calculate ! Vmax, and using your curve, estimate Km. 1/[S] M 8 1/VO (s/UM) 3.85E-03 [S]...
Please mark all that apply, there may be more than one answer for each question, thank...
Please mark all that apply, there may be more than one answer for each question, thank you!: Under which of the following conditions would the Michaelis-Menten equation not hold true? [ ] [S] is constantly changing [ ] [E] is constantly changing [ ] [S] and [P] are constant [ ] [P] is constantly changing Why is it difficult to determine the Vmax from a Michaelis-Menten graph? [ ] It is a complex calculation [ ] Cannot plot a curve...
need B C and D done please please please help!!! 1. You measure the initial rate...
need B C and D done please please please help!!!
1. You measure the initial rate of an enzyme reaction as a function of substrate concentration in the presence and absence of an inhibitor. The following data was obtained: V. (-) Inhibitor (mm/min) (+) Inhibitor (mM/min) 17 [S] (MM) 0.0001 0.0002 0.0005 0.001 0.002 Please submit calculations and graph for full credit! Note: You are required to use Excel to generate the Lineweaver-Burk plot (a) (10 points) Create a Lineweaver-Burk...
12)Show work step by step 13)Show work step by step Below is BoX 6-1 if needed...
12)Show work step by step
13)Show work step by step
Below is BoX 6-1 if needed
Applying the Michaelis-Menten Equation IV An enzyme is found that catalyzes the reaction X= Y Researchers find that the Kyn for the substrate A is 4 pm, and the keat is 20 min . (a) In an experiment, (X) = 6 mm, and the initial velocity, V, was 480 nm min!. What was the (E) used in the experiment? (b) In another experiment, (E)...
Need help with number 13! I already asked about number 12. The inverse velocity and inverse substrate concentration relationship for an enzyme-catalyzed reaction is given below V Vmax Vmax S For the...
Need help with number 13! I already asked about number
12. The inverse velocity and inverse substrate concentration relationship for an enzyme-catalyzed reaction is given below V Vmax Vmax S For the hydration of CO2 catalyzed by carbonic anhydrase, it was determined experimentally that (dm s mol 4023.9+ 39.934 at a total enzyme IS] concentration of 2.32 × 10-y mol-dm- What is the value of the Michaelis constant KM for this enzymatic reaction? (B). 9.92x103 mol dm3 (D). 100.8 mol...
3. Why is an allosteric enzyme more sensitive to substrate concentration around Km values than a Michaelis-Menten enzyme with the same Vmax? 4. Explain how pH and temperature influence enzyme activity. ( A Lineweaver-Burk (double reciprocal) plot was used to compare the effects of three different reversible inhibitors (A, B and C) on an enzyme. The plot of 1/V vs 1/[S] for the enzyme with no inhibitor is shown in a solid black line. The plot of 1/V vs 1/[S]...
Please show work and answer.
my professor gave this hint to us to solve the problem.
He also said that I could find the relationship between S and
Km and substitute that into the Michaelis-Menten equation.
6. The Km of RBC GLUT1 for glucose is 18 mg/dL while the Km for liver GLUT2 is 360 mg/dL. At a blood glucose concentration of 60 mg/dL, GLUT1 and GLUT2 are working at what percentage of their Vmax? A. GLUT1 at 75% Vmax...
That's all the information. Something like this.
Something like this. I don't know why you need more
information.
Its already plotted the (Enzyme) if i cant be answered
close the question, so I may repost it again. Just asked the
professor so i don't know.
6. The Michaelis-Menten curve for enzyme X is shown below for substrate A. Indicate where on the plot you would determine Keat, Kn and kca/Km. 500 1500 2000 1000 substrate A, UM We were unable...
i need help with all question 5 please! thank you
Question 5: Use the data below to construct a Michaelis-Menton curve of velocity vs. [S]. This is quite easy to do in Excel. Vo (UM/s) a) Estimate Vmax from your curve. b) Describe any difficulty you have in completing part (a). Is the enzyme saturated at the highest [S]? c) Using your Vmax estimate, calculate ! Vmax, and using your curve, estimate Km. 1/[S] M 8 1/VO (s/UM) 3.85E-03 [S]...
need B C and D done please please please help!!!
1. You measure the initial rate of an enzyme reaction as a function of substrate concentration in the presence and absence of an inhibitor. The following data was obtained: V. (-) Inhibitor (mm/min) (+) Inhibitor (mM/min) 17 [S] (MM) 0.0001 0.0002 0.0005 0.001 0.002 Please submit calculations and graph for full credit! Note: You are required to use Excel to generate the Lineweaver-Burk plot (a) (10 points) Create a Lineweaver-Burk...
12)Show work step by step
13)Show work step by step
Below is BoX 6-1 if needed
Applying the Michaelis-Menten Equation IV An enzyme is found that catalyzes the reaction X= Y Researchers find that the Kyn for the substrate A is 4 pm, and the keat is 20 min . (a) In an experiment, (X) = 6 mm, and the initial velocity, V, was 480 nm min!. What was the (E) used in the experiment? (b) In another experiment, (E)...
Need help with number 13! I already asked about number
12. The inverse velocity and inverse substrate concentration relationship for an enzyme-catalyzed reaction is given below V Vmax Vmax S For the hydration of CO2 catalyzed by carbonic anhydrase, it was determined experimentally that (dm s mol 4023.9+ 39.934 at a total enzyme IS] concentration of 2.32 × 10-y mol-dm- What is the value of the Michaelis constant KM for this enzymatic reaction? (B). 9.92x103 mol dm3 (D). 100.8 mol...
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